FCG3A_RAT
ID FCG3A_RAT Reviewed; 249 AA.
AC Q6XPU4; A0A0B4J2J1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Low affinity immunoglobulin gamma Fc region receptor III-A {ECO:0000250|UniProtKB:P08637};
DE Short=IgG Fc receptor III-A;
DE AltName: Full=CD16-2 {ECO:0000250|UniProtKB:A0A0B4J1G0};
DE AltName: Full=FcgammaRIV {ECO:0000250|UniProtKB:A0A0B4J1G0};
DE AltName: CD_antigen=CD16a;
DE Flags: Precursor;
GN Name=Fcgr3a {ECO:0000312|RGD:1303067}; Synonyms=Fcgr4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Teusner J.T., Belford D.A., Powell B.C.;
RT "Identification of a novel rat receptor homologous to human FcgammaRIII-
RT A.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NOMENCLATURE.
RX PubMed=7955033;
RA Conrad D., Cooper M., Fridman W.H., Kinet J.P., Ravetch J.;
RT "Nomenclature of Fc receptors. IUIS/WHO Subcommittee on Nomenclature of Fc
RT receptors.";
RL Bull. World Health Organ. 72:809-810(1994).
RN [5]
RP FUNCTION.
RX PubMed=34485821; DOI=10.1093/abt/tbab016;
RA Mao C., Near R., Zhong X., Gao W.;
RT "Cross-species higher sensitivities of FcgammaRIIIA/FcgammaRIV to
RT afucosylated IgG for enhanced ADCC.";
RL Antib Ther 4:159-170(2021).
CC -!- FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin
CC gamma (IgG). Binds with intermediate affinity to both IgG2a and IgG2b.
CC Can bind to IgG2a and IgG2b monomers. Does not display binding to IgG1
CC or IgG3 (By similarity). Recognizes neutralizing virus-specific IgGs
CC displayed on the cell surface of infected cells and triggers antibody-
CC dependent cellular cytotoxicity (ADCC). Confers protection to lethal
CC influenza virus infection (By similarity). On splenic dendritic cells,
CC uptakes antigen immune complexes and efficiently divert them into MHC
CC class I and II antigen presentation pathways to provide for superior
CC priming of CD4-positive and CD8-positive T cell immune responses (By
CC similarity). Mediates neutrophil activation by IgG complexes
CC redundantly with FCGR2A (By similarity). Plays a role in promoting bone
CC resorption by enhancing osteoclast differentiation following binding to
CC IgG2a (By similarity). Also acts as a receptor for the Fc region of
CC immunoglobulin epsilon (IgE). Binds with low affinity to both the a and
CC b allotypes of IgE. Has also been shown to bind to IgE allotype a only
CC but not to allotype b. Binds aggregated IgE but not the monomeric form
CC and bound monomeric IgG is readily displaced by IgE complexes. Binding
CC to IgE promotes macrophage-mediated phagocytosis, antigen presentation
CC to T cells, production of pro-inflammatory cytokines and the late phase
CC of cutaneous allergic reactions (By similarity). Mediates enhanced ADCC
CC in response to afucosylated IgGs (PubMed:34485821).
CC {ECO:0000250|UniProtKB:A0A0B4J1G0, ECO:0000269|PubMed:34485821}.
CC -!- SUBUNIT: Forms a heterooligomeric complex with ITAM-containing
CC signaling subunits FCER1G. Interacts (via transmembrane domain) with
CC signaling subunits; this interaction is a prerequisite for receptor
CC complex expression on the cell surface and intracellular signal
CC transduction. Binds the Fc region of antigen-complexed IgG.
CC {ECO:0000250|UniProtKB:A0A0B4J1G0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A0A0B4J1G0};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:A0A0B4J1G0}.
CC -!- PTM: Phosphorylated following receptor ligation.
CC {ECO:0000250|UniProtKB:A0A0B4J1G0}.
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DR EMBL; AY219230; AAP44530.1; -; mRNA.
DR EMBL; AC111734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473958; EDM09232.1; -; Genomic_DNA.
DR RefSeq; NP_997486.1; NM_207603.1.
DR STRING; 10116.ENSRNOP00000043183; -.
DR GeneID; 304966; -.
DR KEGG; rno:304966; -.
DR CTD; 2214; -.
DR RGD; 1303067; Fcgr3a.
DR eggNOG; ENOG502RU1M; Eukaryota.
DR HOGENOM; CLU_023383_1_0_1; -.
DR OMA; GDNSTQW; -.
DR OrthoDB; 866496at2759; -.
DR PhylomeDB; Q6XPU4; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-2029481; FCGR activation.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-2029485; Role of phospholipids in phagocytosis.
DR Proteomes; UP000002494; Chromosome 13.
DR Proteomes; UP000234681; Chromosome 13.
DR Bgee; ENSRNOG00000024382; Expressed in spleen and 19 other tissues.
DR Genevisible; Q6XPU4; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0033001; C:Fc-gamma receptor III complex; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0019767; F:IgE receptor activity; ISO:RGD.
DR GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR GO; GO:0019770; F:IgG receptor activity; ISO:RGD.
DR GO; GO:0140375; F:immune receptor activity; ISO:RGD.
DR GO; GO:0019772; F:low-affinity IgG receptor activity; ISO:RGD.
DR GO; GO:0001788; P:antibody-dependent cellular cytotoxicity; ISO:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:RGD.
DR GO; GO:0002468; P:dendritic cell antigen processing and presentation; ISO:RGD.
DR GO; GO:0160006; P:Fc receptor-mediated immune complex endocytosis; ISO:RGD.
DR GO; GO:0038094; P:Fc-gamma receptor signaling pathway; ISO:RGD.
DR GO; GO:0042116; P:macrophage activation; ISO:RGD.
DR GO; GO:0030101; P:natural killer cell activation; ISO:RGD.
DR GO; GO:0043320; P:natural killer cell degranulation; ISO:RGD.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:0042119; P:neutrophil activation; ISO:RGD.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0045780; P:positive regulation of bone resorption; ISO:RGD.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; IgE-binding protein;
KW IgG-binding protein; Immunity; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..249
FT /note="Low affinity immunoglobulin gamma Fc region receptor
FT III-A"
FT /evidence="ECO:0000255"
FT /id="PRO_5014221341"
FT TOPO_DOM 21..203
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 31..103
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 117..188
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT SITE 217
FT /note="Important for receptor turnover"
FT /evidence="ECO:0000250|UniProtKB:P08637"
FT MOD_RES 235
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:A0A0B4J1G0"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 46..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 127..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 28
FT /note="N -> I (in Ref. 2; AC111734 and 3; EDM09232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 28168 MW; C58E6B2B97595D21 CRC64;
MWYLLLPTAL LLTVSSGVGA GLQKAVVNLD PEWVRVLEED CVILRCQGTF SPEDNSTKWF
HNKSLISHQD ANYVIQSARV KDSGMYRCQT AFSALSDPVQ LDVHADWLLL QTTKRLFQEG
DPIRLRCHSW RNTPVFKVTY LQNGKGKKYF HRNSELSISK ATHADSGSYF CRGIIGRNNI
SSASLQISIG DPTSPSSFLP WHQITFCLLI GLLFAIDTVL YFSVQRSLQS SVAVYEEPKL
HWSKEPQDK
